Positional and additive effects of basic amino acids on processing of precursor proteins within the constitutive secretory pathway - PubMed (original) (raw)
Positional and additive effects of basic amino acids on processing of precursor proteins within the constitutive secretory pathway
T Watanabe et al. FEBS Lett. 1993.
Free article
Abstract
We have recently shown that the Arg/Lys-X-Lys/Arg-Arg or Arg/Lys-X-X-X-Lys/Arg-Arg sequence serves as a signal for cleavage of precursor proteins within the constitutive secretory pathway, and this cleavage is catalyzed by furin, a mammalian homolog of the yeast Kex2 protease. In this study, we further examined sequence requirements for the constitutive precursor cleavage. Based on the data concerning cleavage efficiencies of various prorenin mutants with amino acid substitution(s) around the native cleavage site expressed in CHO cells, we revised the sequence rules that govern the constitutive cleavage as follows: (i) the Arg residue at position -1 is essential; (ii) in addition to the Arg at position -1, at least two out of the three basic residues at positions -2, -4, and -6 are required for efficient cleavage (the presence of all the three basic residues results in most efficient cleavage); (iii) at position +1, a hydrophobic aliphatic amino acid is not suitable.
Similar articles
- Sequence requirements for precursor cleavage within the constitutive secretory pathway.
Watanabe T, Nakagawa T, Ikemizu J, Nagahama M, Murakami K, Nakayama K. Watanabe T, et al. J Biol Chem. 1992 Apr 25;267(12):8270-4. J Biol Chem. 1992. PMID: 1569080 - Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway.
Hosaka M, Nagahama M, Kim WS, Watanabe T, Hatsuzawa K, Ikemizu J, Murakami K, Nakayama K. Hosaka M, et al. J Biol Chem. 1991 Jul 5;266(19):12127-30. J Biol Chem. 1991. PMID: 1905715 - Sequence requirements for prohormone processing in mouse pituitary AtT-20 cells. Analysis using prorenins as model substrates.
Nagahama M, Nakayama K, Murakami K. Nagahama M, et al. Eur J Biochem. 1991 Apr 10;197(1):135-40. doi: 10.1111/j.1432-1033.1991.tb15891.x. Eur J Biochem. 1991. PMID: 2015816 - Mono- and dibasic proteolytic cleavage sites in insect neuroendocrine peptide precursors.
Veenstra JA. Veenstra JA. Arch Insect Biochem Physiol. 2000 Feb;43(2):49-63. doi: 10.1002/(SICI)1520-6327(200002)43:2<49::AID-ARCH1>3.0.CO;2-M. Arch Insect Biochem Physiol. 2000. PMID: 10644969 Review. - Consensus sequence for processing of peptide precursors at monobasic sites.
Devi L. Devi L. FEBS Lett. 1991 Mar 25;280(2):189-94. doi: 10.1016/0014-5793(91)80290-j. FEBS Lett. 1991. PMID: 2013311 Review.
Cited by
- Thrombin activation of protein C requires prior processing by a liver proprotein convertase.
Essalmani R, Susan-Resiga D, Guillemot J, Kim W, Sachan V, Awan Z, Chamberland A, Asselin MC, Ly K, Desjardins R, Day R, Prat A, Seidah NG. Essalmani R, et al. J Biol Chem. 2017 Jun 23;292(25):10564-10573. doi: 10.1074/jbc.M116.770040. Epub 2017 May 3. J Biol Chem. 2017. PMID: 28468828 Free PMC article. - Effect of C-terminal sequence on competitive semaphorin binding to neuropilin-1.
Parker MW, Linkugel AD, Vander Kooi CW. Parker MW, et al. J Mol Biol. 2013 Nov 15;425(22):4405-14. doi: 10.1016/j.jmb.2013.07.017. Epub 2013 Jul 17. J Mol Biol. 2013. PMID: 23871893 Free PMC article. - Proprotein convertases process Pmel17 during secretion.
Leonhardt RM, Vigneron N, Rahner C, Cresswell P. Leonhardt RM, et al. J Biol Chem. 2011 Mar 18;286(11):9321-37. doi: 10.1074/jbc.M110.168088. Epub 2011 Jan 19. J Biol Chem. 2011. PMID: 21247888 Free PMC article. - Evaluation of germline BMP4 mutation as a cause of colorectal cancer.
Lubbe SJ, Pittman AM, Matijssen C, Twiss P, Olver B, Lloyd A, Qureshi M, Brown N, Nye E, Stamp G, Blagg J, Houlston RS. Lubbe SJ, et al. Hum Mutat. 2011 Jan;32(1):E1928-38. doi: 10.1002/humu.21376. Epub 2010 Oct 14. Hum Mutat. 2011. PMID: 20949628 Free PMC article. - Bridging neuropeptidomics and genomics with bioinformatics: Prediction of mammalian neuropeptide prohormone processing.
Amare A, Hummon AB, Southey BR, Zimmerman TA, Rodriguez-Zas SL, Sweedler JV. Amare A, et al. J Proteome Res. 2006 May;5(5):1162-7. doi: 10.1021/pr0504541. J Proteome Res. 2006. PMID: 16674105 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources